It has been previously shown that most of the human IgG monoclonal D-specif
ic antibodies define a polymorphism in the gorilla consisting of two phenot
ypes: D-gor-positive and D-gor-negative. By quantitative indirect immunoflu
orescence assay and quantitative immunoblotting it was evaluated that the n
umber of D-gor antigenic sites per gorilla red cell varies from a level equ
ivalent to that observed for human RhD positive cells to a level eight time
s higher. By immunoblotting with a rabbit reagent specific for the carboxyl
ic end of human Rh-polypeptides it was demonstrated that RBCs from all gori
llas, whatever their D-gor phenotype, possess 33000 relative molecular mass
Rh-like polypeptides. The expression of the D-gor antigen was shown to be
associated with the presence of three polymorphic bands defined by Southern
blot using a human exon 4 RHCE probe, and to a length polymorphism of gori
lla intron 3 evidenced by polymerase chain reaction. By contrast, the expre
ssion of the D-gor antigen was not associated to the length polymorphism of
gorilla intron 4 which is related to the presence or absence of an Alu-Sx
element in intron 4, paralleling the situation observed in human. These res
ults confirmed the presence in the gorilla genome of at least two RH-like g
enes, one of which being responsible for D-gor polymorphism. The phylogenes
is of the human and gorilla RH genes is discussed in light of the compariso
n of intron 4 sequences.